The effect of p-hydroxyphenylpyruvate, a natural analogue of transketolase substrate, on the catalytic activity of the enzyme was investigated. p-Hydroxyphenylpyruvate proved to be a reversible and competitive inhibitor of transketolase with respect to substrate; it was also able to displace thiamine diphosphate from holotransketolase. The data suggest that p-hydroxyphenylpyruvate participates in the regulation of tyrosine biosynthesis by influencing the catalytic activity of transketolase. Copyright (C) 1999 Federation of European Biochemical Societies.
Solovjeva, O. N., & Kochetov, G. A. (1999). Inhibition of transketolase by p-hydroxyphenylpyruvate. FEBS Letters, 462(3), 246–248. https://doi.org/10.1016/S0014-5793(99)01537-9